Production and characterization of a monoclonal antibody specific for the human lymphocyte low affinity receptor for IgE: CD 23 is a low affinity receptor for IgE.

摘要: In the present study a gamma 1 kappa monoclonal antibody, Mab 25, specific for receptor Fc fragment of IgE on lymphocytes (Fc epsilon RL) was established. This antibody generated after fusion spleen cells from mice immunized with EBV-transformed lymphoblastoid cell line RPMI 8866, which is known to express RL at high density. 25 inhibits strongly binding 8866 and other RL-positive lines. A 50% inhibition observed concentration 10 ng/ml. The also inhibited by Fab fragments suggesting that not simply due steric hindrance or an eventual through its portion. only binds lines expressing RL. immunoprecipitated single polypeptide apparent m.w. 42 Kd, pI 4.9. membrane molecule bound eluted immunoabsorbent had same as purified immunoabsorbent. Additionally, when lysates were cleared no could be found weakly bind minor proportion blood (1 4%), tonsil (2 9%) (4 5%) mononuclear low intensity. By double fluorescence analysis, most CD 20-positive B lymphocytes. staining pattern biochemical characteristics antigen detected comparable those 23 Mab. four MHM 6, PL 13, HD 50, Tu inhibit IgE. 13 totally cells, whereas 6 partially binding. 50 unable block 25. finding different 23/Fc RL-specific antibodies recognizing distinct epitopes have in common capacity inhibiting suggests upon they induce conformational alteration resulting loss capacity. conclusion, our data demonstrate affinity